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Preparation of lyophilized recombinant prion protein for TSE diagnosis by RT-QuIC.

ABSTRACT: OBJECTIVE:Transmissible spongiform encephalopathies (TSEs) are a group of fatal neurodegenerative diseases, often referred as prion diseases. TSEs result from the misfolding of the cellular prion protein (PrPC) into a pathogenic form (PrPSc) that accumulates in the brain and lymphatic tissue. Amplification based assays such as real-time quaking induced conversion allow us to assess the conversion of PrPC to PrPSc. Real-time quaking induced conversion (RT-QuIC) can be used for the detection of PrPSc in a variety of biological tissues from humans and animals. However, RT-QuIC requires a continuous supply of freshly purified prion protein and this necessity is not sustainable in a diagnostic laboratory setting. RESULTS:In this study, we developed a method to dry and preserve the prion protein for long term storage allowing for production of the protein and storage for extended time prior to use and room temperature shipping to appropriate diagnostic laboratory destinations facilitating widespread use of RT-QuIC as a diagnostic method.

SUBMITTER: Hwang S 

PROVIDER: S-EPMC6295004 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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Preparation of lyophilized recombinant prion protein for TSE diagnosis by RT-QuIC.

Hwang Soyoun S   Tatum Trudy T   Lebepe-Mazur Semakaleng S   Nicholson Eric M EM  

BMC research notes 20181214 1

<h4>Objective</h4>Transmissible spongiform encephalopathies (TSEs) are a group of fatal neurodegenerative diseases, often referred as prion diseases. TSEs result from the misfolding of the cellular prion protein (PrP<sup>C</sup>) into a pathogenic form (PrP<sup>Sc</sup>) that accumulates in the brain and lymphatic tissue. Amplification based assays such as real-time quaking induced conversion allow us to assess the conversion of PrP<sup>C</sup> to PrP<sup>Sc</sup>. Real-time quaking induced conv  ...[more]

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